Analysis of the Cooperativity of Human β-Cell Glucokinase through the Stimulatory Effect of Glucose on Fructose Phosphorylation

Journal of Biological Chemistry

Volumn 276, Issue 6, 2001, Pages 3872-3878

  Moukil, Moulay A ^b   Van Schaftingen, Emile ^a  

^a UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; COMPUTER SIMULATION; CONFORMATIONS; ESCHERICHIA COLI; FRUCTOSE; GLUCOSE; MUTAGENESIS; PHOSPHATES;

PHOSPHORYLATION;

ENZYMES;

FRUCTOSE; FRUCTOSE 6 PHOSPHATE; GLUCOKINASE; GLUCOSE; MANNOHEPTULOSE; N ACETYLGLUCOSAMINE; PALMITOYL COENZYME A;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; HUMAN; PANCREAS ISLET BETA CELL; PHOSPHORYLATION; POINT MUTATION; PRIORITY JOURNAL; REGULATORY MECHANISM; ENZYMOLOGY; METABOLISM; PANCREAS ISLET;

ESCHERICHIA COLI;

CATALYTIC DOMAIN; FRUCTOSE; GLUCOKINASE; GLUCOSE; HUMANS; ISLETS OF LANGERHANS; PHOSPHORYLATION; SUBSTRATE SPECIFICITY;

EID: 0035830927     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M008722200     Document Type: Article

References (34)

1. Randle, P. J. (1993) Diabetologia 36, 269-275
2. Matschinsky, F. M. (1996) Diabetes 45, 223-241
3. Parry, M. J., and Walker, D. G. (1966) Biochem. J. 99, 266-274
4. Niemeyer, H., Cardenas, M. L., Rabajille, E., Ureta, T., Clarck-Turri, L., and Penaranda, J. (1975) Enzyme 20, 321-333
5. Storer, A. C., and Cornish-Bowden, A. (1976) Biochem. J. 159, 7-14
6. Monod, J., Wyman, J., and Changeux, J. P. (1965) J. Mol. Biol. 12, 88-118
7. Koshland, D. E., Némethy, G., and Filmer, D. (1966) Biochemistry 5, 365-385
8. Cardenas, M. L., Rabajille, E., and Niemeyer, H. (1978) Arch. Biochem. Biophys. 190, 142-148
9. Ferdinand, W. (1966) Biochem. J. 98, 278-283
10. Cornish-Bowden, A., and Storer, A. C. (1986) Biochem. J. 240, 293-296
11. Storer, A. C., and Cornish-Bowden, A. (1977) Biochem. J. 165, 61-69
12. Cardenas, M. L., Rabajille, E., and Niemeyer, H. (1984) Biochem. J. 222, 363-370
13. Pollard-Knight, D., and Cornish-Bowden, A. (1987) Biochem. J. 245, 625-629
14. Neet, K. E., Keenan, R. P., and Tippett, P. S. (1990) Biochemistry 29, 770-777
15. Lin, S. X., and Neet, K. E. (1990) J. Biol. Chem. 265, 9670-9675
16. Cornish-Bowden, A., and Cardenas, M. L. (1987) J. Theor. Biol. 124, 1-23
17. Connolly, B. A., and Trayer, I. P. (1979) Eur. J. Biochem. 99, 299-308
18. Agius, L., and Stubbs, M. (2000) Biochem. J. 346, 413-421
19. Scruel, O., Sener, A., and Malaisse, W. J. (1997) Mol. Cell. Biochem. 175, 263-269
20. Tiedge, M., Richter, T., and Lenzen, S. (2000) Arch. Biochem. Biophys. 375, 251-260
21. Veiga-da-Cunha, M., Detheux, M., Watelet, N., and Van Schaftingen, E. (1994) Eur. J. Biochem. 225, 43-51
22. Moukil, M. A., Veiga-da-Cunha, M., and Van Schaftingen, E. (2000) Diabetes 49, 195-201
23. Veiga-da-Cunha, M., Xu, L. Z., Lee, Y. H., Marotta, D., Pilkis, S. J., and Van Schaftingen, E. Diabetologia 39, 1173-1179
24. Yamada, M., and Saier, M. H., Jr. (1987) J. Biol. Chem. 262, 5455-5463
25. Studier, F. W., and Moffatt, B. A. (1986) J. Mol. Biol. 189, 113-130
26. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254
27. Bergmeyer, H. U. (1988) in Methods of Enzymatic Analysis (Bergmeyer, J., and Grassl, M., eds) 3rd Ed., Vol. VI, pp. 169-170, Verlag Chemie, Weinheim, Germany
28. Dawson, C. M., and Hales, C. N. (1969) Biochim. Biophys. Acta 176, 657-659
29. Tippett, P. S., and Neet, K. E. (1982) J. Biol. Chem. 257, 12839-12845
30. St. Charles, R., Harrison, R. W., Bell, G. I., Pilkis, S. J., and Weber, I. T. (1994) Diabetes 43, 784-791
31. Xu, L. Z., Zhang, W., Weber, I. T., Harrison, R. W., and Pilkis, S. J. (1994) J. Biol. Chem. 269, 27458-27465
32. Pettersson, G. (1986) Eur. J. Biochem. 154, 167-170
33. Anderson, C. M., Stenkamp, R. E., McDonald, R. C., and Steitz, T. A. (1978) J. Mol. Biol. 123, 207-219
34. Aleshin, A. E., Zeng, C., Bartunik, H. D., Fromm, H. J., and Honzatko, R. B. (1998) J. Mol. Biol. 282, 345-357